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- W116752875 abstract "The crystal structure of γ-aminobutyric acid aminotransferase (GABA-AT) from pig liver has been solved by molecular replacement at 3.0 A resolution. In the brain, the enzyme catalyzes the degradation of the major inhibitory neurotransmitter GABA and is a recognized target for anticonvulsant drugs. The fold of the dimeric enzyme is similar to that of ornithine aminotransferase (OAT), dialkylglycine decarboxylase (DGD) and glutamate-l-semialdehyde aminomutase (GSAT). In the active site, the cofactor is covalently bound as an internal alditnine of pyridoxal phosphate and Lys329. The binding pocket of GABA-AT shows several structural homologies with that of OAT, with the exception of two side chain replacements which should be responsible for the distinct substrate specificities. Considering the high sequence identity with the human enzyme (96%) this structure represents a valuable target for the development of new anticonvulsant drugs." @default.
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- W116752875 date "2000-01-01" @default.
- W116752875 modified "2023-09-25" @default.
- W116752875 title "GABA-aminotransferase, a target for antiepileptic drug therapy" @default.
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- W116752875 doi "https://doi.org/10.1007/978-3-0348-8397-9_52" @default.
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